PDZ、SH3结构域结合特性的研究
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摘要
蛋白质在细胞的生命活动中扮演着重要角色,但是,其功能的发挥却并非依靠单个蛋白质独立的作用。它们在细胞中通常与其他蛋白质相互作用形成大的复合体,在特定的时间和空间内完成特定的功能,蛋白质之间的相互作用才是蛋白质执行其功能的途径。
本论文主要研究了介导蛋白质相互作用网络的PDZ结构域和SH3结构域的结合特性。
本文研究了PDLIM2蛋白中的PDZ结构域的结合特性。利用酵母双杂交技术筛选随机多肽文库,我们验证了PDLIM2-PDZ可识别x-x-W-L配体；此外还发现了K-H-K-V配体,是对PDLIM2-PDZ蛋白识别规律的补充。
论文第二部分研究了PDZK2蛋白中PDZ1的结合特性。根据PDZK2 PDZ1结构域与PDZK1 PDZ1同源的性质,我们直接利用酵母双杂交技术筛选构建的PDZ配体库来研究PDZK2 PDZ1的结合特性。验证筛选方法较常规文库筛选具有高效性和针对性,可以快速研究相关结构域的结合特性。验证筛选文库相对于其他文库筛选方法可以得到除阳性配体外的阴性序列,并且阴性序列和阳性配体对比总结可以得到更全面的结合特性。
论文第三部分成功构建新型非脯氨酸的随机多肽文库。我们尝试利用新型文库研究结合非脯氨酸的SH3结构域的结合特性,发现了FYN SH3结构域的一个非脯氨酸结合序列VSLVKLFF。
Proteins play important functions. But their functions can not be performed by a single protein alone. Proteins are usually associated with other in cells to form protein-protein complexes.
This thesis studies the binding characteristics of the PDZ domain and SH3 domain, which mediates protein-protein interaction network.
The PDLIM2 PDZ's binding characteristics were studied using yeast two-hybrid screening of random peptide library. x-x-W-L and K-H-K-V were found to be the concensuses of the binding sequences. This prompts that PDLIM2-PDZ protein may play different roles in different systems.
With the knowledge that PDZK2 PDZ1 domain is homologous to PDZK1 PDZ1, we screened the class one peptide library for PDZK2 PDZ1's by yeast two-hybrid validation. The overall efficiency is dramatically improved compare to traditional screening. The results showed the sequences of both binding and unbinding clones.
A non-proline random peptide librarie was constructed to study the SH3 domain binding characteristics. A non-proline ligand VSLVKLFF was found by screening the library with FYN SH3 domain.
本论文主要研究了介导蛋白质相互作用网络的PDZ结构域和SH3结构域的结合特性。
本文研究了PDLIM2蛋白中的PDZ结构域的结合特性。利用酵母双杂交技术筛选随机多肽文库,我们验证了PDLIM2-PDZ可识别x-x-W-L配体；此外还发现了K-H-K-V配体,是对PDLIM2-PDZ蛋白识别规律的补充。
论文第二部分研究了PDZK2蛋白中PDZ1的结合特性。根据PDZK2 PDZ1结构域与PDZK1 PDZ1同源的性质,我们直接利用酵母双杂交技术筛选构建的PDZ配体库来研究PDZK2 PDZ1的结合特性。验证筛选方法较常规文库筛选具有高效性和针对性,可以快速研究相关结构域的结合特性。验证筛选文库相对于其他文库筛选方法可以得到除阳性配体外的阴性序列,并且阴性序列和阳性配体对比总结可以得到更全面的结合特性。
论文第三部分成功构建新型非脯氨酸的随机多肽文库。我们尝试利用新型文库研究结合非脯氨酸的SH3结构域的结合特性,发现了FYN SH3结构域的一个非脯氨酸结合序列VSLVKLFF。
Proteins play important functions. But their functions can not be performed by a single protein alone. Proteins are usually associated with other in cells to form protein-protein complexes.
This thesis studies the binding characteristics of the PDZ domain and SH3 domain, which mediates protein-protein interaction network.
The PDLIM2 PDZ's binding characteristics were studied using yeast two-hybrid screening of random peptide library. x-x-W-L and K-H-K-V were found to be the concensuses of the binding sequences. This prompts that PDLIM2-PDZ protein may play different roles in different systems.
With the knowledge that PDZK2 PDZ1 domain is homologous to PDZK1 PDZ1, we screened the class one peptide library for PDZK2 PDZ1's by yeast two-hybrid validation. The overall efficiency is dramatically improved compare to traditional screening. The results showed the sequences of both binding and unbinding clones.
A non-proline random peptide librarie was constructed to study the SH3 domain binding characteristics. A non-proline ligand VSLVKLFF was found by screening the library with FYN SH3 domain.
引文
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